大鼠胰抑制素合成C末端片段对内分泌胰腺的生物活性

Bioactivity of synthetic C-terminal fragment of rat pancreastatin on endocrine pancreas.

作者信息

Funakoshi A, Miyasaka K, Kitani K, Tamamura H, Funakoshi S, Yajima H

机构信息

National Kyushu Cancer Center, Fukuoka, Japan.

出版信息

Biochem Biophys Res Commun. 1989 Feb 15;158(3):844-9. doi: 10.1016/0006-291x(89)92799-x.

DOI:10.1016/0006-291x(89)92799-x

PMID:2645871

Abstract

A C-terminal fragment of rat pancreastatin, 26-residue peptide amide was synthesized by the Fmoc-based solid phase method and its biological activity was evaluated for the first time in the conscious rat. Rat pancreastatin inhibited glucose-stimulated insulin secretion and elevated blood glucose levels in a concentration of 10 nmol/kg/h. The relative molar potency of that of porcine is equivalent. This study suggests that the synthetic rat pancreastatin has a biological activity, and may play a physiological role in the endocrine pancreas.

摘要

采用基于Fmoc的固相法合成了大鼠胰抑制素的C末端片段（一种26个残基的肽酰胺），并首次在清醒大鼠中评估了其生物活性。大鼠胰抑制素以10 nmol/kg/h的浓度抑制葡萄糖刺激的胰岛素分泌并升高血糖水平。其相对摩尔效力与猪胰抑制素相当。本研究表明，合成的大鼠胰抑制素具有生物活性，可能在内分泌胰腺中发挥生理作用。